Ribonuclease sensitivity of Escherichia coli ribosomes.
Santer, Melvin (Haverford College, Haverford, Pa.), and Josephine R. Smith. Ribonuclease sensitivity of Escherichia coli ribosomes. J. Bacteriol. 92:1099-1110. 1966.-The ribonucleic acid (RNA) contained in 70S ribosomes and in 50S and 30S subunits was hydrolyzed by pancreatic ribonuclease. A 7% amount of the RNA was removed from the 70S particle; at 10(-4)m magnesium concentration, a maximum of 24 and 30% of the RNA in the 50S and the 30S fractions, respectively, was removed by ribonuclease. At the two lower magnesium ion concentrations, 50S ribosomes did not lose any protein, whereas 30S ribosomes lost protein as a result of ribonuclease treatment. A number of proteins were removed from the 30S particles by ribonuclease, and these proteins were antigenically related to proteins present in 50S ribosomes. The differential effect of ribonuclease on 50S and 30S ribosomes suggested that they have structural dissimilarities.
D001426:Bacterial Proteins / Q000032:analysis; D004926:Escherichia coli; D007118:Immunoassay; D008274:Magnesium / Q000494:pharmacology; D008320:Maltose; D010759:Phosphorus Isotopes; D012329:RNA, Bacterial / Q000378:metabolism; D012260:Ribonucleases / Q000494:pharmacology*; D012270:Ribosomes / Q000032:analysis*; D013460:Sulfur Isotopes
D001426:Bacterial Proteins; D010759:Phosphorus Isotopes; D012329:RNA, Bacterial; D013460:Sulfur Isotopes; D008320:Maltose; D012260:Ribonucleases; D008274:Magnesium